HEADER IMMUNE SYSTEM 09-APR-20 6YMQ TITLE TREM2 EXTRACELLULAR DOMAIN (19-131) IN COMPLEX WITH SINGLE-CHAIN TITLE 2 VARIABLE 4 (SCFV-4) COMPND MOL_ID: 1; COMPND 2 MOLECULE: SINGLE-CHAIN VARIABLE 4; COMPND 3 CHAIN: A, B, C, D, E, F; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: TRIGGERING RECEPTOR EXPRESSED ON MYELOID CELLS 2; COMPND 7 CHAIN: G, H, I, J, K, D000; COMPND 8 SYNONYM: TREM-2,TRIGGERING RECEPTOR EXPRESSED ON MONOCYTES 2; COMPND 9 ENGINEERED: YES; COMPND 10 OTHER_DETAILS: N-ACETYLGLUCOSAMINE NAG SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: TREM2; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL: EXPI293F; SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PHL-SEC KEYWDS SCFV, COMPLEX, RECEPTOR, ALZHEIMER'S, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.SZYKOWSKA,C.PREGER,A.SCACIOC,S.M.M.MUKHOPADHYAY,G.MCKINLEY, AUTHOR 2 S.GRASLUND,E.WIGREN,H.PERSSON,F.VON DELFT,C.H.ARROWSMITH,A.EDWARDS, AUTHOR 3 C.BOUNTRA,E.DI DANIEL,J.B.DAVIS,N.BURGESS-BROWN,A.BULLOCK JRNL AUTH A.SZYKOWSKA,Y.CHEN,T.B.SMITH,C.PREGER,J.YANG,D.QIAN, JRNL AUTH 2 S.M.MUKHOPADHYAY,E.WIGREN,S.J.NEAME,S.GRASLUND,H.PERSSON, JRNL AUTH 3 P.J.ATKINSON,E.DI DANIEL,E.MEAD,J.WANG,J.B.DAVIS, JRNL AUTH 4 N.A.BURGESS-BROWN,A.N.BULLOCK JRNL TITL SELECTION AND STRUCTURAL CHARACTERIZATION OF ANTI-TREM2 JRNL TITL 2 SCFVS THAT REDUCE LEVELS OF SHED ECTODOMAIN. JRNL REF STRUCTURE 2021 JRNL REFN ISSN 0969-2126 JRNL PMID 34233201 JRNL DOI 10.1016/J.STR.2021.06.010 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.SZYKOWSKA,Y.CHEN,T.B.SMITH,C.PREGER,J.YANG,D.QIAN, REMARK 1 AUTH 2 S.MUKHOPADHYAY,E.WIGREN,S.J.NEAME,S.GRASLUND,H.PERSSON, REMARK 1 AUTH 3 P.J.ATKINSON,E.DI DANIEL,E.MEAD,J.WANG,J.B.DAVIS, REMARK 1 AUTH 4 N.A.BURGESS-BROWN,A.N.BULLOCK REMARK 1 TITL SELECTION AND STRUCTURAL CHARACTERISATION OF ANTI-TREM2 REMARK 1 TITL 2 SCFVS THAT REDUCE LEVELS OF SHED ECTODOMAIN REMARK 1 REF BIORXIV 2021 REMARK 1 REFN REMARK 1 DOI 10.1101/2021.02.07.430123 REMARK 2 REMARK 2 RESOLUTION. 3.07 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.17.1_3660 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.07 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 75.99 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 71715 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.274 REMARK 3 R VALUE (WORKING SET) : 0.274 REMARK 3 FREE R VALUE : 0.288 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 3515 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 83.7500 - 8.9700 0.99 2915 150 0.2526 0.2376 REMARK 3 2 8.9700 - 7.1200 1.00 2796 165 0.2457 0.2682 REMARK 3 3 7.1200 - 6.2200 1.00 2794 129 0.2609 0.2781 REMARK 3 4 6.2200 - 5.6500 1.00 2757 143 0.2513 0.2529 REMARK 3 5 5.6500 - 5.2500 1.00 2749 134 0.2571 0.3198 REMARK 3 6 5.2500 - 4.9400 1.00 2766 142 0.2243 0.2472 REMARK 3 7 4.9400 - 4.6900 1.00 2739 130 0.2186 0.2274 REMARK 3 8 4.6900 - 4.4900 1.00 2708 158 0.2289 0.2431 REMARK 3 9 4.4900 - 4.3200 1.00 2701 155 0.2402 0.2468 REMARK 3 10 4.3200 - 4.1700 1.00 2753 124 0.2438 0.2921 REMARK 3 11 4.1700 - 4.0400 1.00 2726 136 0.2648 0.2659 REMARK 3 12 4.0400 - 3.9200 1.00 2696 147 0.2833 0.3154 REMARK 3 13 3.9200 - 3.8200 1.00 2700 152 0.2854 0.2924 REMARK 3 14 3.8200 - 3.7200 1.00 2698 153 0.2904 0.3060 REMARK 3 15 3.7200 - 3.6400 1.00 2695 151 0.3140 0.3376 REMARK 3 16 3.6400 - 3.5600 1.00 2721 128 0.3190 0.3242 REMARK 3 17 3.5600 - 3.4900 1.00 2693 121 0.3069 0.3109 REMARK 3 18 3.4900 - 3.4300 1.00 2717 129 0.3185 0.3310 REMARK 3 19 3.4300 - 3.3600 1.00 2745 127 0.3305 0.3448 REMARK 3 20 3.3600 - 3.3100 1.00 2673 156 0.3405 0.3586 REMARK 3 21 3.3100 - 3.2500 1.00 2703 134 0.3455 0.3588 REMARK 3 22 3.2500 - 3.2000 1.00 2676 137 0.3644 0.3560 REMARK 3 23 3.2000 - 3.1600 1.00 2707 131 0.3741 0.3547 REMARK 3 24 3.1600 - 3.1100 1.00 2669 146 0.3861 0.4088 REMARK 3 25 3.1100 - 3.0700 1.00 2703 137 0.4072 0.4564 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.439 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.331 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 69.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 88.14 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.001 16085 REMARK 3 ANGLE : 0.392 21846 REMARK 3 CHIRALITY : 0.038 2381 REMARK 3 PLANARITY : 0.003 2781 REMARK 3 DIHEDRAL : 12.245 5605 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 12 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN 'J' AND RESID 20 THROUGH 131) REMARK 3 ORIGIN FOR THE GROUP (A): 76.5096 17.0538 113.2228 REMARK 3 T TENSOR REMARK 3 T11: 0.4049 T22: 0.4550 REMARK 3 T33: 0.4983 T12: -0.0098 REMARK 3 T13: 0.0577 T23: -0.0396 REMARK 3 L TENSOR REMARK 3 L11: 0.6707 L22: 1.5513 REMARK 3 L33: 7.2235 L12: -0.0220 REMARK 3 L13: 0.2754 L23: -0.4599 REMARK 3 S TENSOR REMARK 3 S11: 0.0385 S12: -0.1336 S13: -0.0306 REMARK 3 S21: 0.0927 S22: -0.1091 S23: 0.0892 REMARK 3 S31: -0.5826 S32: -0.1400 S33: 0.0886 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'G' AND RESID 20 THROUGH 131) REMARK 3 ORIGIN FOR THE GROUP (A): 67.7960 5.3535 25.8750 REMARK 3 T TENSOR REMARK 3 T11: 0.2861 T22: 0.4486 REMARK 3 T33: 0.5187 T12: -0.0544 REMARK 3 T13: -0.0313 T23: 0.0279 REMARK 3 L TENSOR REMARK 3 L11: 2.4913 L22: 1.0798 REMARK 3 L33: 7.9778 L12: -0.3563 REMARK 3 L13: -1.1169 L23: 0.3532 REMARK 3 S TENSOR REMARK 3 S11: 0.0958 S12: -0.0942 S13: -0.0660 REMARK 3 S21: 0.0212 S22: 0.0347 S23: -0.0037 REMARK 3 S31: -0.2164 S32: 0.2324 S33: -0.1405 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'H' AND RESID 20 THROUGH 131) REMARK 3 ORIGIN FOR THE GROUP (A): 87.4827 23.2560 25.8276 REMARK 3 T TENSOR REMARK 3 T11: 0.4935 T22: 0.3869 REMARK 3 T33: 0.4892 T12: 0.0206 REMARK 3 T13: 0.1333 T23: -0.0431 REMARK 3 L TENSOR REMARK 3 L11: 3.9833 L22: 3.4221 REMARK 3 L33: 5.5521 L12: 0.1234 REMARK 3 L13: 3.5726 L23: 1.3511 REMARK 3 S TENSOR REMARK 3 S11: 0.1603 S12: 0.3502 S13: -0.3120 REMARK 3 S21: 0.4237 S22: 0.0974 S23: -0.1451 REMARK 3 S31: 0.1117 S32: 0.3658 S33: -0.2803 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN 'K' AND RESID 20 THROUGH 131) REMARK 3 ORIGIN FOR THE GROUP (A): 80.5103 77.3974 47.3876 REMARK 3 T TENSOR REMARK 3 T11: 1.8921 T22: 0.7025 REMARK 3 T33: 1.1976 T12: -0.1551 REMARK 3 T13: 0.1572 T23: -0.0328 REMARK 3 L TENSOR REMARK 3 L11: 1.1267 L22: 0.6610 REMARK 3 L33: 1.6927 L12: -0.5558 REMARK 3 L13: -0.0552 L23: 0.0253 REMARK 3 S TENSOR REMARK 3 S11: -0.2943 S12: -0.1582 S13: 0.5771 REMARK 3 S21: -1.1945 S22: 0.1715 S23: 0.2267 REMARK 3 S31: -0.4378 S32: -0.1930 S33: 0.1912 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN 'L' AND RESID 20 THROUGH 131) REMARK 3 ORIGIN FOR THE GROUP (A): 11.5111 -0.0470 42.0744 REMARK 3 T TENSOR REMARK 3 T11: 0.6453 T22: 1.5258 REMARK 3 T33: 1.1500 T12: -0.0463 REMARK 3 T13: -0.0391 T23: 0.2811 REMARK 3 L TENSOR REMARK 3 L11: 0.4586 L22: 1.6049 REMARK 3 L33: 0.7482 L12: -0.5052 REMARK 3 L13: -0.4592 L23: -0.0818 REMARK 3 S TENSOR REMARK 3 S11: -0.0720 S12: 1.3114 S13: 0.3657 REMARK 3 S21: 0.2168 S22: -0.2444 S23: 0.4453 REMARK 3 S31: -0.1798 S32: 0.0087 S33: 0.3021 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN 'I' AND RESID 20 THROUGH 131) REMARK 3 ORIGIN FOR THE GROUP (A): 66.5362 -7.0905 112.9389 REMARK 3 T TENSOR REMARK 3 T11: 0.3883 T22: 0.7077 REMARK 3 T33: 0.4836 T12: -0.1237 REMARK 3 T13: 0.0145 T23: 0.0695 REMARK 3 L TENSOR REMARK 3 L11: 2.2109 L22: 1.9129 REMARK 3 L33: 3.3906 L12: -0.1717 REMARK 3 L13: 1.8337 L23: 0.6608 REMARK 3 S TENSOR REMARK 3 S11: -0.2067 S12: -0.2857 S13: 0.0521 REMARK 3 S21: 0.2392 S22: 0.1827 S23: 0.1560 REMARK 3 S31: 0.1589 S32: -0.7499 S33: 0.0321 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 3 THROUGH 245) REMARK 3 ORIGIN FOR THE GROUP (A): 50.8664 6.7624 51.9344 REMARK 3 T TENSOR REMARK 3 T11: 0.5571 T22: 1.1416 REMARK 3 T33: 0.4748 T12: 0.1055 REMARK 3 T13: -0.0196 T23: 0.1194 REMARK 3 L TENSOR REMARK 3 L11: 2.8349 L22: 1.3549 REMARK 3 L33: 1.8165 L12: -0.0217 REMARK 3 L13: 0.6944 L23: -0.5989 REMARK 3 S TENSOR REMARK 3 S11: -0.0250 S12: -0.2153 S13: 0.0857 REMARK 3 S21: 0.2460 S22: 0.1893 S23: 0.1503 REMARK 3 S31: -0.4693 S32: -1.2886 S33: -0.1239 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (CHAIN 'B' AND RESID 3 THROUGH 245) REMARK 3 ORIGIN FOR THE GROUP (A): 52.9844 -13.5000 86.0551 REMARK 3 T TENSOR REMARK 3 T11: 0.5849 T22: 1.2669 REMARK 3 T33: 0.6189 T12: -0.3693 REMARK 3 T13: -0.1028 T23: 0.1225 REMARK 3 L TENSOR REMARK 3 L11: 2.5916 L22: 1.8895 REMARK 3 L33: 0.7132 L12: 0.7265 REMARK 3 L13: -0.3649 L23: 0.4964 REMARK 3 S TENSOR REMARK 3 S11: 0.0860 S12: -0.0054 S13: -0.3162 REMARK 3 S21: -0.1145 S22: -0.0674 S23: 0.3452 REMARK 3 S31: 0.5054 S32: -1.4388 S33: 0.0118 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: (CHAIN 'C' AND RESID 3 THROUGH 245) REMARK 3 ORIGIN FOR THE GROUP (A): 69.4353 31.8475 87.2846 REMARK 3 T TENSOR REMARK 3 T11: 1.3360 T22: 0.6937 REMARK 3 T33: 0.5671 T12: 0.3485 REMARK 3 T13: -0.0143 T23: 0.0313 REMARK 3 L TENSOR REMARK 3 L11: 1.6979 L22: 3.4440 REMARK 3 L33: 1.4500 L12: -0.4971 REMARK 3 L13: 0.4887 L23: 0.3673 REMARK 3 S TENSOR REMARK 3 S11: -0.2741 S12: -0.1104 S13: 0.3155 REMARK 3 S21: 0.0660 S22: 0.0972 S23: 0.3302 REMARK 3 S31: -1.7741 S32: -0.7181 S33: 0.1380 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: (CHAIN 'D' AND RESID 3 THROUGH 245) REMARK 3 ORIGIN FOR THE GROUP (A): 89.3670 37.4077 53.3796 REMARK 3 T TENSOR REMARK 3 T11: 1.5743 T22: 0.4881 REMARK 3 T33: 0.5512 T12: -0.2299 REMARK 3 T13: -0.0118 T23: 0.0105 REMARK 3 L TENSOR REMARK 3 L11: 0.6269 L22: 2.0486 REMARK 3 L33: 0.8010 L12: 0.3770 REMARK 3 L13: 0.3195 L23: -0.4858 REMARK 3 S TENSOR REMARK 3 S11: -0.0377 S12: -0.1796 S13: 0.1365 REMARK 3 S21: 0.4194 S22: -0.0378 S23: -0.1714 REMARK 3 S31: -1.4232 S32: 0.1448 S33: 0.0711 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: (CHAIN 'E' AND RESID 3 THROUGH 245) REMARK 3 ORIGIN FOR THE GROUP (A): 27.8987 4.9281 16.3319 REMARK 3 T TENSOR REMARK 3 T11: 0.3400 T22: 2.5187 REMARK 3 T33: 0.7365 T12: 0.0990 REMARK 3 T13: -0.1962 T23: 0.4009 REMARK 3 L TENSOR REMARK 3 L11: 2.2233 L22: 0.8646 REMARK 3 L33: 1.0545 L12: -0.2340 REMARK 3 L13: 0.6246 L23: -0.1265 REMARK 3 S TENSOR REMARK 3 S11: -0.0213 S12: 0.2794 S13: -0.0729 REMARK 3 S21: -0.2607 S22: 0.2459 S23: 0.3642 REMARK 3 S31: -0.3218 S32: -1.6551 S33: 0.0910 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: (CHAIN 'F' AND RESID 3 THROUGH 245) REMARK 3 ORIGIN FOR THE GROUP (A): 87.4950 63.8828 19.9167 REMARK 3 T TENSOR REMARK 3 T11: 2.6550 T22: 0.3250 REMARK 3 T33: 0.7115 T12: -0.4991 REMARK 3 T13: 0.0146 T23: 0.2258 REMARK 3 L TENSOR REMARK 3 L11: 1.5269 L22: 1.9250 REMARK 3 L33: 0.7888 L12: 0.1297 REMARK 3 L13: -0.1887 L23: -0.1478 REMARK 3 S TENSOR REMARK 3 S11: -0.0407 S12: 0.4841 S13: 0.2686 REMARK 3 S21: 0.8468 S22: -0.3281 S23: -0.2454 REMARK 3 S31: -1.4384 S32: 0.1788 S33: 0.0273 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6YMQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292106968. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-MAY-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9688 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS REMARK 200 DATA SCALING SOFTWARE : DIALS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71788 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.070 REMARK 200 RESOLUTION RANGE LOW (A) : 83.750 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 6.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.8300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.07 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.18 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 6.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 1.16_3549 REMARK 200 STARTING MODEL: 6G8R 5UD7 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 68.64 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.92 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 39% MPD -- 0.2M AMMONIUM ACETATE -- REMARK 280 0.1M CITRATE PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X+1/2,Y+1/2,-Z REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 83.75500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 90.38500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 83.75500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 90.38500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1700 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15040 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1750 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15070 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, I REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1960 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15040 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, J REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2260 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15010 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 5 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1810 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15100 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 6 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2000 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15500 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D000, E REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER A 1 REMARK 465 MET A 2 REMARK 465 GLY A 124 REMARK 465 GLY A 125 REMARK 465 GLY A 126 REMARK 465 GLY A 127 REMARK 465 SER A 128 REMARK 465 GLY A 129 REMARK 465 GLY A 130 REMARK 465 GLY A 131 REMARK 465 GLY A 132 REMARK 465 SER A 133 REMARK 465 GLY A 134 REMARK 465 GLY A 135 REMARK 465 GLY A 136 REMARK 465 GLY A 137 REMARK 465 SER B 1 REMARK 465 MET B 2 REMARK 465 GLY B 124 REMARK 465 GLY B 125 REMARK 465 GLY B 126 REMARK 465 GLY B 127 REMARK 465 SER B 128 REMARK 465 GLY B 129 REMARK 465 GLY B 130 REMARK 465 GLY B 131 REMARK 465 GLY B 132 REMARK 465 SER B 133 REMARK 465 GLY B 134 REMARK 465 GLY B 135 REMARK 465 GLY B 136 REMARK 465 GLY B 137 REMARK 465 SER B 138 REMARK 465 SER C 1 REMARK 465 MET C 2 REMARK 465 GLY C 124 REMARK 465 GLY C 125 REMARK 465 GLY C 126 REMARK 465 GLY C 127 REMARK 465 SER C 128 REMARK 465 GLY C 129 REMARK 465 GLY C 130 REMARK 465 GLY C 131 REMARK 465 GLY C 132 REMARK 465 SER C 133 REMARK 465 GLY C 134 REMARK 465 GLY C 135 REMARK 465 GLY C 136 REMARK 465 GLY C 137 REMARK 465 LYS C 245 REMARK 465 SER D 1 REMARK 465 GLY D 124 REMARK 465 GLY D 125 REMARK 465 GLY D 126 REMARK 465 GLY D 127 REMARK 465 SER D 128 REMARK 465 GLY D 129 REMARK 465 GLY D 130 REMARK 465 GLY D 131 REMARK 465 GLY D 132 REMARK 465 SER D 133 REMARK 465 GLY D 134 REMARK 465 GLY D 135 REMARK 465 GLY D 136 REMARK 465 GLY D 137 REMARK 465 LYS D 245 REMARK 465 GLU G 16 REMARK 465 THR G 17 REMARK 465 GLY G 18 REMARK 465 GLY G 132 REMARK 465 THR G 133 REMARK 465 LYS G 134 REMARK 465 HIS G 135 REMARK 465 HIS G 136 REMARK 465 HIS G 137 REMARK 465 HIS G 138 REMARK 465 HIS G 139 REMARK 465 HIS G 140 REMARK 465 GLU H 16 REMARK 465 THR H 17 REMARK 465 GLY H 18 REMARK 465 HIS H 19 REMARK 465 GLY H 132 REMARK 465 THR H 133 REMARK 465 LYS H 134 REMARK 465 HIS H 135 REMARK 465 HIS H 136 REMARK 465 HIS H 137 REMARK 465 HIS H 138 REMARK 465 HIS H 139 REMARK 465 HIS H 140 REMARK 465 GLU I 16 REMARK 465 THR I 17 REMARK 465 GLY I 18 REMARK 465 GLY I 132 REMARK 465 THR I 133 REMARK 465 LYS I 134 REMARK 465 HIS I 135 REMARK 465 HIS I 136 REMARK 465 HIS I 137 REMARK 465 HIS I 138 REMARK 465 HIS I 139 REMARK 465 HIS I 140 REMARK 465 GLU J 16 REMARK 465 THR J 17 REMARK 465 GLY J 18 REMARK 465 HIS J 19 REMARK 465 GLY J 132 REMARK 465 THR J 133 REMARK 465 LYS J 134 REMARK 465 HIS J 135 REMARK 465 HIS J 136 REMARK 465 HIS J 137 REMARK 465 HIS J 138 REMARK 465 HIS J 139 REMARK 465 HIS J 140 REMARK 465 GLU K 16 REMARK 465 THR K 17 REMARK 465 GLY K 18 REMARK 465 ASP K 131 REMARK 465 GLY K 132 REMARK 465 THR K 133 REMARK 465 LYS K 134 REMARK 465 HIS K 135 REMARK 465 HIS K 136 REMARK 465 HIS K 137 REMARK 465 HIS K 138 REMARK 465 HIS K 139 REMARK 465 HIS K 140 REMARK 465 GLU D 16 REMARK 465 THR D 17 REMARK 465 GLY D 18 REMARK 465 HIS D 19 REMARK 465 GLY D 132 REMARK 465 THR D 133 REMARK 465 LYS D 134 REMARK 465 HIS D 135 REMARK 465 HIS D 136 REMARK 465 HIS D 137 REMARK 465 HIS D 138 REMARK 465 HIS D 139 REMARK 465 HIS D 140 REMARK 465 SER E 1 REMARK 465 GLY E 124 REMARK 465 GLY E 125 REMARK 465 GLY E 126 REMARK 465 GLY E 127 REMARK 465 SER E 128 REMARK 465 GLY E 129 REMARK 465 GLY E 130 REMARK 465 GLY E 131 REMARK 465 GLY E 132 REMARK 465 SER E 133 REMARK 465 GLY E 134 REMARK 465 GLY E 135 REMARK 465 GLY E 136 REMARK 465 GLY E 137 REMARK 465 SER F 1 REMARK 465 MET F 2 REMARK 465 GLY F 124 REMARK 465 GLY F 125 REMARK 465 GLY F 126 REMARK 465 GLY F 127 REMARK 465 SER F 128 REMARK 465 GLY F 129 REMARK 465 GLY F 130 REMARK 465 GLY F 131 REMARK 465 GLY F 132 REMARK 465 SER F 133 REMARK 465 GLY F 134 REMARK 465 GLY F 135 REMARK 465 GLY F 136 REMARK 465 GLY F 137 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLN A 15 CG CD OE1 NE2 REMARK 470 LYS A 67 CG CD CE NZ REMARK 470 ILE A 140 CG1 CG2 CD1 REMARK 470 SER A 145 OG REMARK 470 SER A 148 OG REMARK 470 VAL A 157 CG1 CG2 REMARK 470 THR A 158 OG1 CG2 REMARK 470 ARG A 162 NH1 NH2 REMARK 470 LYS A 183 CG CD CE NZ REMARK 470 LYS A 241 CG CD CE NZ REMARK 470 SER B 23 OG REMARK 470 ASP B 64 OD1 OD2 REMARK 470 LYS B 67 NZ REMARK 470 LYS B 78 NZ REMARK 470 SER B 152 OG REMARK 470 LYS B 183 CE NZ REMARK 470 ILE B 213 CD1 REMARK 470 PHE B 221 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG B 230 NH1 REMARK 470 LYS B 245 CG CD CE NZ REMARK 470 SER C 147 OG REMARK 470 SER C 148 OG REMARK 470 LEU C 149 CG CD1 CD2 REMARK 470 LYS C 180 CD CE NZ REMARK 470 LYS C 183 CE NZ REMARK 470 LEU C 216 CD1 CD2 REMARK 470 LYS C 241 CG CD CE NZ REMARK 470 LEU C 242 CG CD1 CD2 REMARK 470 MET D 2 CG SD CE REMARK 470 SER D 138 N CB OG REMARK 470 GLN D 141 CG CD OE1 NE2 REMARK 470 SER D 148 OG REMARK 470 LEU D 149 CG CD1 CD2 REMARK 470 VAL D 157 CG1 CG2 REMARK 470 SER D 190 OG REMARK 470 GLU D 219 CG CD OE1 OE2 REMARK 470 GLN D 228 CG CD OE1 NE2 REMARK 470 LYS D 241 CG CD CE NZ REMARK 470 HIS G 19 CG ND1 CD2 CE1 NE2 REMARK 470 HIS I 19 CG ND1 CD2 CE1 NE2 REMARK 470 LYS J 42 NZ REMARK 470 GLU J 56 CG CD OE1 OE2 REMARK 470 LYS J 57 CG CD CE NZ REMARK 470 ARG J 77 CG CD NE CZ NH1 NH2 REMARK 470 HIS K 19 CG ND1 CD2 CE1 NE2 REMARK 470 GLN K 30 CG CD OE1 NE2 REMARK 470 LYS K 42 CG CD CE NZ REMARK 470 LYS K 57 CG CD CE NZ REMARK 470 ASN K 68 CG OD1 ND2 REMARK 470 LEU K 69 CG CD1 CD2 REMARK 470 SER K 81 OG REMARK 470 LEU K 89 CG CD1 CD2 REMARK 470 THR K 92 OG1 CG2 REMARK 470 THR K 94 OG1 CG2 REMARK 470 THR K 96 OG1 CG2 REMARK 470 ARG K 98 CG CD NE CZ NH1 NH2 REMARK 470 THR D 22 OG1 CG2 REMARK 470 ARG D 47 CG CD NE CZ NH1 NH2 REMARK 470 ARG D 76 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 123 CG CD CE NZ REMARK 470 MET E 2 CG SD CE REMARK 470 GLU E 3 CG CD OE1 OE2 REMARK 470 LEU E 13 CG CD1 CD2 REMARK 470 LEU E 20 CG CD1 CD2 REMARK 470 LYS E 45 CG CD CE NZ REMARK 470 SER E 51 OG REMARK 470 LYS E 67 CG CD CE NZ REMARK 470 THR E 71 OG1 CG2 REMARK 470 ARG E 74 CG CD NE CZ NH1 NH2 REMARK 470 LEU E 83 CG CD1 CD2 REMARK 470 GLN E 84 CG CD OE1 NE2 REMARK 470 MET E 85 CG SD CE REMARK 470 ARG E 89 CG CD NE CZ NH1 NH2 REMARK 470 GLU E 91 CG CD OE1 OE2 REMARK 470 ASP E 92 CG OD1 OD2 REMARK 470 GLN E 115 CG CD OE1 NE2 REMARK 470 LEU E 118 CG CD1 CD2 REMARK 470 VAL E 119 CG1 CG2 REMARK 470 ASP E 139 CG OD1 OD2 REMARK 470 GLN E 165 CG CD OE1 NE2 REMARK 470 SER E 168 OG REMARK 470 SER E 190 OG REMARK 470 LEU F 7 CG CD1 CD2 REMARK 470 GLN F 15 CG CD OE1 NE2 REMARK 470 TYR F 59 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS F 67 CG CD CE NZ REMARK 470 ILE F 72 CG1 CG2 CD1 REMARK 470 ARG F 74 CG CD NE CZ NH1 NH2 REMARK 470 LYS F 78 CG CD CE NZ REMARK 470 ILE F 140 CG1 CG2 CD1 REMARK 470 GLN F 165 CG CD OE1 NE2 REMARK 470 LEU F 233 CG CD1 CD2 REMARK 470 LYS F 245 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 VAL A 50 -77.54 -97.54 REMARK 500 TYR A 103 111.86 -33.90 REMARK 500 TYR A 105 -63.19 -125.62 REMARK 500 SER A 108 -164.97 -100.95 REMARK 500 CYS A 161 117.90 -162.85 REMARK 500 SER A 168 -136.74 59.22 REMARK 500 TYR A 170 79.04 -118.30 REMARK 500 LEU A 185 -74.26 -108.89 REMARK 500 ALA A 189 -53.75 68.08 REMARK 500 SER A 190 13.75 -140.94 REMARK 500 SER A 214 -70.34 -61.05 REMARK 500 THR B 30 98.70 -68.39 REMARK 500 VAL B 50 -80.28 -96.93 REMARK 500 TYR B 103 113.15 -34.65 REMARK 500 TYR B 105 -65.18 -130.19 REMARK 500 SER B 108 -165.84 -100.66 REMARK 500 SER B 122 -150.02 -126.84 REMARK 500 SER B 168 -129.55 59.79 REMARK 500 ALA B 189 -50.40 67.73 REMARK 500 SER B 190 31.36 -141.66 REMARK 500 SER B 231 -167.54 -104.84 REMARK 500 GLU B 243 -168.64 -123.21 REMARK 500 THR C 30 98.39 -67.85 REMARK 500 PRO C 43 105.73 -59.18 REMARK 500 VAL C 50 -73.15 -91.09 REMARK 500 SER C 57 17.19 59.84 REMARK 500 LEU C 83 89.84 -151.46 REMARK 500 TYR C 103 113.44 -34.62 REMARK 500 TYR C 105 -65.14 -132.41 REMARK 500 SER C 108 -166.17 -100.90 REMARK 500 VAL C 121 -63.98 -90.58 REMARK 500 SER C 122 -132.82 58.14 REMARK 500 PRO C 146 94.42 -68.92 REMARK 500 SER C 168 -150.97 60.23 REMARK 500 LEU C 185 -64.35 -108.90 REMARK 500 ALA C 189 -53.86 65.18 REMARK 500 ALA C 222 -166.47 -160.26 REMARK 500 ARG C 230 -40.61 -130.07 REMARK 500 VAL D 50 -75.16 -100.29 REMARK 500 SER D 57 15.85 59.75 REMARK 500 TYR D 103 110.72 -33.95 REMARK 500 TYR D 105 -65.46 -130.09 REMARK 500 SER D 108 -165.86 -100.66 REMARK 500 SER D 122 -158.10 -97.90 REMARK 500 SER D 168 -129.06 59.85 REMARK 500 TYR D 170 78.14 -107.35 REMARK 500 LEU D 185 -70.96 -109.31 REMARK 500 ALA D 189 -53.95 65.70 REMARK 500 ALA D 222 -165.86 -161.18 REMARK 500 ARG D 230 -35.12 -130.14 REMARK 500 REMARK 500 THIS ENTRY HAS 100 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 GLY G 201 REMARK 610 NAG G 202 REMARK 610 NAG I 201 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6Y6C RELATED DB: PDB REMARK 900 CONTAINS THE SAME SUBUNITS REMARK 900 RELATED ID: 6YMQ RELATED DB: PDB REMARK 900 CONTAIN THE SAME COMPONENTS DBREF 6YMQ A 1 245 PDB 6YMQ 6YMQ 1 245 DBREF 6YMQ B 1 245 PDB 6YMQ 6YMQ 1 245 DBREF 6YMQ C 1 245 PDB 6YMQ 6YMQ 1 245 DBREF 6YMQ D 1 245 PDB 6YMQ 6YMQ 1 245 DBREF 6YMQ G 19 131 UNP Q9NZC2 TREM2_HUMAN 19 131 DBREF 6YMQ H 19 131 UNP Q9NZC2 TREM2_HUMAN 19 131 DBREF 6YMQ I 19 131 UNP Q9NZC2 TREM2_HUMAN 19 131 DBREF 6YMQ J 19 131 UNP Q9NZC2 TREM2_HUMAN 19 131 DBREF 6YMQ K 19 131 UNP Q9NZC2 TREM2_HUMAN 19 131 DBREF 6YMQ00 19 131 UNP Q9NZC2 TREM2_HUMAN 19 131 DBREF 6YMQ E 1 245 PDB 6YMQ 6YMQ 1 245 DBREF 6YMQ F 1 245 PDB 6YMQ 6YMQ 1 245 SEQADV 6YMQ GLU G 16 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ THR G 17 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ GLY G 18 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ GLY G 132 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ THR G 133 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ LYS G 134 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS G 135 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS G 136 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS G 137 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS G 138 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS G 139 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS G 140 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ GLU H 16 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ THR H 17 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ GLY H 18 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ GLY H 132 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ THR H 133 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ LYS H 134 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS H 135 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS H 136 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS H 137 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS H 138 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS H 139 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS H 140 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ GLU I 16 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ THR I 17 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ GLY I 18 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ GLY I 132 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ THR I 133 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ LYS I 134 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS I 135 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS I 136 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS I 137 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS I 138 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS I 139 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS I 140 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ GLU J 16 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ THR J 17 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ GLY J 18 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ GLY J 132 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ THR J 133 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ LYS J 134 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS J 135 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS J 136 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS J 137 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS J 138 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS J 139 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS J 140 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ GLU K 16 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ THR K 17 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ GLY K 18 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ GLY K 132 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ THR K 133 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ LYS K 134 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS K 135 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS K 136 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS K 137 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS K 138 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS K 139 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS K 140 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ GLU00 16 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ THR00 17 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ GLY00 18 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ GLY00 132 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ THR00 133 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ LYS00 134 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS00 135 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS00 136 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS00 137 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS00 138 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS00 139 UNP Q9NZC2 EXPRESSION TAG SEQADV 6YMQ HIS00 140 UNP Q9NZC2 EXPRESSION TAG SEQRES 1 A 245 SER MET GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU SEQRES 2 A 245 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 A 245 SER GLY PHE THR PHE SER TYR TYR TYR MET GLY TRP VAL SEQRES 4 A 245 ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY SEQRES 5 A 245 ILE SER PRO SER SER GLY TYR THR TYR TYR ALA ASP SER SEQRES 6 A 245 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS SEQRES 7 A 245 ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU SEQRES 8 A 245 ASP THR ALA VAL TYR TYR CYS ALA ARG TYR TYR TYR GLY SEQRES 9 A 245 TYR TYR TYR SER HIS MET ASP TYR TRP GLY GLN GLY THR SEQRES 10 A 245 LEU VAL THR VAL SER SER GLY GLY GLY GLY SER GLY GLY SEQRES 11 A 245 GLY GLY SER GLY GLY GLY GLY SER ASP ILE GLN MET THR SEQRES 12 A 245 GLN SER PRO SER SER LEU SER ALA SER VAL GLY ASP ARG SEQRES 13 A 245 VAL THR ILE THR CYS ARG ALA SER GLN SER ILE SER SER SEQRES 14 A 245 TYR LEU ASN TRP TYR GLN GLN LYS PRO GLY LYS ALA PRO SEQRES 15 A 245 LYS LEU LEU ILE TYR ALA ALA SER SER LEU GLN SER GLY SEQRES 16 A 245 VAL PRO SER ARG PHE SER GLY SER GLY SER GLY THR ASP SEQRES 17 A 245 PHE THR LEU THR ILE SER SER LEU GLN PRO GLU ASP PHE SEQRES 18 A 245 ALA THR TYR TYR CYS GLN GLN SER ARG SER GLY LEU HIS SEQRES 19 A 245 THR PHE GLY GLN GLY THR LYS LEU GLU ILE LYS SEQRES 1 B 245 SER MET GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU SEQRES 2 B 245 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 B 245 SER GLY PHE THR PHE SER TYR TYR TYR MET GLY TRP VAL SEQRES 4 B 245 ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY SEQRES 5 B 245 ILE SER PRO SER SER GLY TYR THR TYR TYR ALA ASP SER SEQRES 6 B 245 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS SEQRES 7 B 245 ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU SEQRES 8 B 245 ASP THR ALA VAL TYR TYR CYS ALA ARG TYR TYR TYR GLY SEQRES 9 B 245 TYR TYR TYR SER HIS MET ASP TYR TRP GLY GLN GLY THR SEQRES 10 B 245 LEU VAL THR VAL SER SER GLY GLY GLY GLY SER GLY GLY SEQRES 11 B 245 GLY GLY SER GLY GLY GLY GLY SER ASP ILE GLN MET THR SEQRES 12 B 245 GLN SER PRO SER SER LEU SER ALA SER VAL GLY ASP ARG SEQRES 13 B 245 VAL THR ILE THR CYS ARG ALA SER GLN SER ILE SER SER SEQRES 14 B 245 TYR LEU ASN TRP TYR GLN GLN LYS PRO GLY LYS ALA PRO SEQRES 15 B 245 LYS LEU LEU ILE TYR ALA ALA SER SER LEU GLN SER GLY SEQRES 16 B 245 VAL PRO SER ARG PHE SER GLY SER GLY SER GLY THR ASP SEQRES 17 B 245 PHE THR LEU THR ILE SER SER LEU GLN PRO GLU ASP PHE SEQRES 18 B 245 ALA THR TYR TYR CYS GLN GLN SER ARG SER GLY LEU HIS SEQRES 19 B 245 THR PHE GLY GLN GLY THR LYS LEU GLU ILE LYS SEQRES 1 C 245 SER MET GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU SEQRES 2 C 245 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 C 245 SER GLY PHE THR PHE SER TYR TYR TYR MET GLY TRP VAL SEQRES 4 C 245 ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY SEQRES 5 C 245 ILE SER PRO SER SER GLY TYR THR TYR TYR ALA ASP SER SEQRES 6 C 245 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS SEQRES 7 C 245 ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU SEQRES 8 C 245 ASP THR ALA VAL TYR TYR CYS ALA ARG TYR TYR TYR GLY SEQRES 9 C 245 TYR TYR TYR SER HIS MET ASP TYR TRP GLY GLN GLY THR SEQRES 10 C 245 LEU VAL THR VAL SER SER GLY GLY GLY GLY SER GLY GLY SEQRES 11 C 245 GLY GLY SER GLY GLY GLY GLY SER ASP ILE GLN MET THR SEQRES 12 C 245 GLN SER PRO SER SER LEU SER ALA SER VAL GLY ASP ARG SEQRES 13 C 245 VAL THR ILE THR CYS ARG ALA SER GLN SER ILE SER SER SEQRES 14 C 245 TYR LEU ASN TRP TYR GLN GLN LYS PRO GLY LYS ALA PRO SEQRES 15 C 245 LYS LEU LEU ILE TYR ALA ALA SER SER LEU GLN SER GLY SEQRES 16 C 245 VAL PRO SER ARG PHE SER GLY SER GLY SER GLY THR ASP SEQRES 17 C 245 PHE THR LEU THR ILE SER SER LEU GLN PRO GLU ASP PHE SEQRES 18 C 245 ALA THR TYR TYR CYS GLN GLN SER ARG SER GLY LEU HIS SEQRES 19 C 245 THR PHE GLY GLN GLY THR LYS LEU GLU ILE LYS SEQRES 1 D 245 SER MET GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU SEQRES 2 D 245 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 D 245 SER GLY PHE THR PHE SER TYR TYR TYR MET GLY TRP VAL SEQRES 4 D 245 ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY SEQRES 5 D 245 ILE SER PRO SER SER GLY TYR THR TYR TYR ALA ASP SER SEQRES 6 D 245 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS SEQRES 7 D 245 ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU SEQRES 8 D 245 ASP THR ALA VAL TYR TYR CYS ALA ARG TYR TYR TYR GLY SEQRES 9 D 245 TYR TYR TYR SER HIS MET ASP TYR TRP GLY GLN GLY THR SEQRES 10 D 245 LEU VAL THR VAL SER SER GLY GLY GLY GLY SER GLY GLY SEQRES 11 D 245 GLY GLY SER GLY GLY GLY GLY SER ASP ILE GLN MET THR SEQRES 12 D 245 GLN SER PRO SER SER LEU SER ALA SER VAL GLY ASP ARG SEQRES 13 D 245 VAL THR ILE THR CYS ARG ALA SER GLN SER ILE SER SER SEQRES 14 D 245 TYR LEU ASN TRP TYR GLN GLN LYS PRO GLY LYS ALA PRO SEQRES 15 D 245 LYS LEU LEU ILE TYR ALA ALA SER SER LEU GLN SER GLY SEQRES 16 D 245 VAL PRO SER ARG PHE SER GLY SER GLY SER GLY THR ASP SEQRES 17 D 245 PHE THR LEU THR ILE SER SER LEU GLN PRO GLU ASP PHE SEQRES 18 D 245 ALA THR TYR TYR CYS GLN GLN SER ARG SER GLY LEU HIS SEQRES 19 D 245 THR PHE GLY GLN GLY THR LYS LEU GLU ILE LYS SEQRES 1 G 125 GLU THR GLY HIS ASN THR THR VAL PHE GLN GLY VAL ALA SEQRES 2 G 125 GLY GLN SER LEU GLN VAL SER CYS PRO TYR ASP SER MET SEQRES 3 G 125 LYS HIS TRP GLY ARG ARG LYS ALA TRP CYS ARG GLN LEU SEQRES 4 G 125 GLY GLU LYS GLY PRO CYS GLN ARG VAL VAL SER THR HIS SEQRES 5 G 125 ASN LEU TRP LEU LEU SER PHE LEU ARG ARG TRP ASN GLY SEQRES 6 G 125 SER THR ALA ILE THR ASP ASP THR LEU GLY GLY THR LEU SEQRES 7 G 125 THR ILE THR LEU ARG ASN LEU GLN PRO HIS ASP ALA GLY SEQRES 8 G 125 LEU TYR GLN CYS GLN SER LEU HIS GLY SER GLU ALA ASP SEQRES 9 G 125 THR LEU ARG LYS VAL LEU VAL GLU VAL LEU ALA ASP GLY SEQRES 10 G 125 THR LYS HIS HIS HIS HIS HIS HIS SEQRES 1 H 125 GLU THR GLY HIS ASN THR THR VAL PHE GLN GLY VAL ALA SEQRES 2 H 125 GLY GLN SER LEU GLN VAL SER CYS PRO TYR ASP SER MET SEQRES 3 H 125 LYS HIS TRP GLY ARG ARG LYS ALA TRP CYS ARG GLN LEU SEQRES 4 H 125 GLY GLU LYS GLY PRO CYS GLN ARG VAL VAL SER THR HIS SEQRES 5 H 125 ASN LEU TRP LEU LEU SER PHE LEU ARG ARG TRP ASN GLY SEQRES 6 H 125 SER THR ALA ILE THR ASP ASP THR LEU GLY GLY THR LEU SEQRES 7 H 125 THR ILE THR LEU ARG ASN LEU GLN PRO HIS ASP ALA GLY SEQRES 8 H 125 LEU TYR GLN CYS GLN SER LEU HIS GLY SER GLU ALA ASP SEQRES 9 H 125 THR LEU ARG LYS VAL LEU VAL GLU VAL LEU ALA ASP GLY SEQRES 10 H 125 THR LYS HIS HIS HIS HIS HIS HIS SEQRES 1 I 125 GLU THR GLY HIS ASN THR THR VAL PHE GLN GLY VAL ALA SEQRES 2 I 125 GLY GLN SER LEU GLN VAL SER CYS PRO TYR ASP SER MET SEQRES 3 I 125 LYS HIS TRP GLY ARG ARG LYS ALA TRP CYS ARG GLN LEU SEQRES 4 I 125 GLY GLU LYS GLY PRO CYS GLN ARG VAL VAL SER THR HIS SEQRES 5 I 125 ASN LEU TRP LEU LEU SER PHE LEU ARG ARG TRP ASN GLY SEQRES 6 I 125 SER THR ALA ILE THR ASP ASP THR LEU GLY GLY THR LEU SEQRES 7 I 125 THR ILE THR LEU ARG ASN LEU GLN PRO HIS ASP ALA GLY SEQRES 8 I 125 LEU TYR GLN CYS GLN SER LEU HIS GLY SER GLU ALA ASP SEQRES 9 I 125 THR LEU ARG LYS VAL LEU VAL GLU VAL LEU ALA ASP GLY SEQRES 10 I 125 THR LYS HIS HIS HIS HIS HIS HIS SEQRES 1 J 125 GLU THR GLY HIS ASN THR THR VAL PHE GLN GLY VAL ALA SEQRES 2 J 125 GLY GLN SER LEU GLN VAL SER CYS PRO TYR ASP SER MET SEQRES 3 J 125 LYS HIS TRP GLY ARG ARG LYS ALA TRP CYS ARG GLN LEU SEQRES 4 J 125 GLY GLU LYS GLY PRO CYS GLN ARG VAL VAL SER THR HIS SEQRES 5 J 125 ASN LEU TRP LEU LEU SER PHE LEU ARG ARG TRP ASN GLY SEQRES 6 J 125 SER THR ALA ILE THR ASP ASP THR LEU GLY GLY THR LEU SEQRES 7 J 125 THR ILE THR LEU ARG ASN LEU GLN PRO HIS ASP ALA GLY SEQRES 8 J 125 LEU TYR GLN CYS GLN SER LEU HIS GLY SER GLU ALA ASP SEQRES 9 J 125 THR LEU ARG LYS VAL LEU VAL GLU VAL LEU ALA ASP GLY SEQRES 10 J 125 THR LYS HIS HIS HIS HIS HIS HIS SEQRES 1 K 125 GLU THR GLY HIS ASN THR THR VAL PHE GLN GLY VAL ALA SEQRES 2 K 125 GLY GLN SER LEU GLN VAL SER CYS PRO TYR ASP SER MET SEQRES 3 K 125 LYS HIS TRP GLY ARG ARG LYS ALA TRP CYS ARG GLN LEU SEQRES 4 K 125 GLY GLU LYS GLY PRO CYS GLN ARG VAL VAL SER THR HIS SEQRES 5 K 125 ASN LEU TRP LEU LEU SER PHE LEU ARG ARG TRP ASN GLY SEQRES 6 K 125 SER THR ALA ILE THR ASP ASP THR LEU GLY GLY THR LEU SEQRES 7 K 125 THR ILE THR LEU ARG ASN LEU GLN PRO HIS ASP ALA GLY SEQRES 8 K 125 LEU TYR GLN CYS GLN SER LEU HIS GLY SER GLU ALA ASP SEQRES 9 K 125 THR LEU ARG LYS VAL LEU VAL GLU VAL LEU ALA ASP GLY SEQRES 10 K 125 THR LYS HIS HIS HIS HIS HIS HIS SEQRES 100 125 GLU THR GLY HIS ASN THR THR VAL PHE GLN GLY VAL ALA SEQRES 200 125 GLY GLN SER LEU GLN VAL SER CYS PRO TYR ASP SER MET SEQRES 300 125 LYS HIS TRP GLY ARG ARG LYS ALA TRP CYS ARG GLN LEU SEQRES 400 125 GLY GLU LYS GLY PRO CYS GLN ARG VAL VAL SER THR HIS SEQRES 500 125 ASN LEU TRP LEU LEU SER PHE LEU ARG ARG TRP ASN GLY SEQRES 600 125 SER THR ALA ILE THR ASP ASP THR LEU GLY GLY THR LEU SEQRES 700 125 THR ILE THR LEU ARG ASN LEU GLN PRO HIS ASP ALA GLY SEQRES 800 125 LEU TYR GLN CYS GLN SER LEU HIS GLY SER GLU ALA ASP SEQRES 900 125 THR LEU ARG LYS VAL LEU VAL GLU VAL LEU ALA ASP GLY SEQRES 1000 125 THR LYS HIS HIS HIS HIS HIS HIS SEQRES 1 E 245 SER MET GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU SEQRES 2 E 245 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 E 245 SER GLY PHE THR PHE SER TYR TYR TYR MET GLY TRP VAL SEQRES 4 E 245 ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY SEQRES 5 E 245 ILE SER PRO SER SER GLY TYR THR TYR TYR ALA ASP SER SEQRES 6 E 245 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS SEQRES 7 E 245 ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU SEQRES 8 E 245 ASP THR ALA VAL TYR TYR CYS ALA ARG TYR TYR TYR GLY SEQRES 9 E 245 TYR TYR TYR SER HIS MET ASP TYR TRP GLY GLN GLY THR SEQRES 10 E 245 LEU VAL THR VAL SER SER GLY GLY GLY GLY SER GLY GLY SEQRES 11 E 245 GLY GLY SER GLY GLY GLY GLY SER ASP ILE GLN MET THR SEQRES 12 E 245 GLN SER PRO SER SER LEU SER ALA SER VAL GLY ASP ARG SEQRES 13 E 245 VAL THR ILE THR CYS ARG ALA SER GLN SER ILE SER SER SEQRES 14 E 245 TYR LEU ASN TRP TYR GLN GLN LYS PRO GLY LYS ALA PRO SEQRES 15 E 245 LYS LEU LEU ILE TYR ALA ALA SER SER LEU GLN SER GLY SEQRES 16 E 245 VAL PRO SER ARG PHE SER GLY SER GLY SER GLY THR ASP SEQRES 17 E 245 PHE THR LEU THR ILE SER SER LEU GLN PRO GLU ASP PHE SEQRES 18 E 245 ALA THR TYR TYR CYS GLN GLN SER ARG SER GLY LEU HIS SEQRES 19 E 245 THR PHE GLY GLN GLY THR LYS LEU GLU ILE LYS SEQRES 1 F 245 SER MET GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU SEQRES 2 F 245 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 F 245 SER GLY PHE THR PHE SER TYR TYR TYR MET GLY TRP VAL SEQRES 4 F 245 ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY SEQRES 5 F 245 ILE SER PRO SER SER GLY TYR THR TYR TYR ALA ASP SER SEQRES 6 F 245 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS SEQRES 7 F 245 ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU SEQRES 8 F 245 ASP THR ALA VAL TYR TYR CYS ALA ARG TYR TYR TYR GLY SEQRES 9 F 245 TYR TYR TYR SER HIS MET ASP TYR TRP GLY GLN GLY THR SEQRES 10 F 245 LEU VAL THR VAL SER SER GLY GLY GLY GLY SER GLY GLY SEQRES 11 F 245 GLY GLY SER GLY GLY GLY GLY SER ASP ILE GLN MET THR SEQRES 12 F 245 GLN SER PRO SER SER LEU SER ALA SER VAL GLY ASP ARG SEQRES 13 F 245 VAL THR ILE THR CYS ARG ALA SER GLN SER ILE SER SER SEQRES 14 F 245 TYR LEU ASN TRP TYR GLN GLN LYS PRO GLY LYS ALA PRO SEQRES 15 F 245 LYS LEU LEU ILE TYR ALA ALA SER SER LEU GLN SER GLY SEQRES 16 F 245 VAL PRO SER ARG PHE SER GLY SER GLY SER GLY THR ASP SEQRES 17 F 245 PHE THR LEU THR ILE SER SER LEU GLN PRO GLU ASP PHE SEQRES 18 F 245 ALA THR TYR TYR CYS GLN GLN SER ARG SER GLY LEU HIS SEQRES 19 F 245 THR PHE GLY GLN GLY THR LYS LEU GLU ILE LYS HET GLY G 201 4 HET NAG G 202 14 HET NAG H 201 14 HET NAG I 201 14 HET NAG J 201 14 HET MPD J 202 8 HET NAG K 201 14 HET NAG 00 201 14 HETNAM GLY GLYCINE HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL FORMUL 13 GLY C2 H5 N O2 FORMUL 14 NAG 6(C8 H15 N O6) FORMUL 18 MPD C6 H14 O2 FORMUL 21 HOH *13(H2 O) HELIX 1 AA1 ARG A 89 THR A 93 5 5 HELIX 2 AA2 ARG B 89 THR B 93 5 5 HELIX 3 AA3 GLN B 217 PHE B 221 5 5 HELIX 4 AA4 ARG C 89 THR C 93 5 5 HELIX 5 AA5 ARG D 89 THR D 93 5 5 HELIX 6 AA6 GLN D 217 PHE D 221 5 5 HELIX 7 AA7 LEU G 69 SER G 73 5 5 HELIX 8 AA8 GLN G 101 ALA G 105 5 5 HELIX 9 AA9 LEU H 69 SER H 73 5 5 HELIX 10 AB1 GLN H 101 ALA H 105 5 5 HELIX 11 AB2 LEU I 69 SER I 73 5 5 HELIX 12 AB3 GLN I 101 ALA I 105 5 5 HELIX 13 AB4 LEU J 69 SER J 73 5 5 HELIX 14 AB5 GLN J 101 ALA J 105 5 5 HELIX 15 AB6 LEU K 69 SER K 73 5 5 HELIX 16 AB7 GLN00 101 ALA00 105 5 5 HELIX 17 AB8 GLN E 217 PHE E 221 5 5 SHEET 1 A 4 GLN A 5 SER A 9 0 SHEET 2 A 4 LEU A 20 SER A 27 -1 SHEET 3 A 4 THR A 80 MET A 85 -1 SHEET 4 A 4 PHE A 70 ASP A 75 -1 SHEET 1 B 6 GLY A 12 GLN A 15 0 SHEET 2 B 6 THR A 117 SER A 122 1 SHEET 3 B 6 ALA A 94 ARG A 100 -1 SHEET 4 B 6 MET A 36 GLN A 41 -1 SHEET 5 B 6 LEU A 47 ILE A 53 -1 SHEET 6 B 6 THR A 60 TYR A 62 -1 SHEET 1 C 2 SER A 148 SER A 150 0 SHEET 2 C 2 LYS A 241 GLU A 243 1 SHEET 1 D 3 VAL A 157 ARG A 162 0 SHEET 2 D 3 ASP A 208 ILE A 213 -1 SHEET 3 D 3 PHE A 200 SER A 205 -1 SHEET 1 E 3 THR A 223 GLN A 228 0 SHEET 2 E 3 LEU A 171 GLN A 176 -1 SHEET 3 E 3 LYS A 183 ILE A 186 -1 SHEET 1 F 2 ALA A 99 TYR A 101 0 SHEET 2 F 2 MET A 110 TRP A 113 -1 SHEET 1 G 4 GLN B 5 SER B 9 0 SHEET 2 G 4 LEU B 20 SER B 27 -1 SHEET 3 G 4 THR B 80 MET B 85 -1 SHEET 4 G 4 PHE B 70 ASP B 75 -1 SHEET 1 H 6 GLY B 12 GLN B 15 0 SHEET 2 H 6 THR B 117 SER B 122 1 SHEET 3 H 6 ALA B 94 ARG B 100 -1 SHEET 4 H 6 MET B 36 GLN B 41 -1 SHEET 5 H 6 LEU B 47 ILE B 53 -1 SHEET 6 H 6 THR B 60 TYR B 62 -1 SHEET 1 I 4 MET B 142 GLN B 144 0 SHEET 2 I 4 VAL B 157 ALA B 163 -1 SHEET 3 I 4 ASP B 208 ILE B 213 -1 SHEET 4 I 4 PHE B 200 SER B 205 -1 SHEET 1 J 2 SER B 148 ALA B 151 0 SHEET 2 J 2 LYS B 241 ILE B 244 1 SHEET 1 K 3 THR B 223 GLN B 228 0 SHEET 2 K 3 LEU B 171 GLN B 176 -1 SHEET 3 K 3 LYS B 183 ILE B 186 -1 SHEET 1 L 2 ALA B 99 TYR B 101 0 SHEET 2 L 2 MET B 110 TRP B 113 -1 SHEET 1 M 4 GLN C 5 SER C 9 0 SHEET 2 M 4 LEU C 20 SER C 27 -1 SHEET 3 M 4 THR C 80 MET C 85 -1 SHEET 4 M 4 PHE C 70 ASP C 75 -1 SHEET 1 N 5 THR C 117 VAL C 119 0 SHEET 2 N 5 ALA C 94 ARG C 100 -1 SHEET 3 N 5 MET C 36 ALA C 42 -1 SHEET 4 N 5 LEU C 47 ILE C 53 -1 SHEET 5 N 5 THR C 60 TYR C 62 -1 SHEET 1 O 4 MET C 142 GLN C 144 0 SHEET 2 O 4 VAL C 157 ALA C 163 -1 SHEET 3 O 4 ASP C 208 ILE C 213 -1 SHEET 4 O 4 PHE C 200 SER C 205 -1 SHEET 1 P 3 THR C 223 GLN C 228 0 SHEET 2 P 3 LEU C 171 GLN C 176 -1 SHEET 3 P 3 LYS C 183 ILE C 186 -1 SHEET 1 Q 2 ALA C 99 TYR C 101 0 SHEET 2 Q 2 MET C 110 TRP C 113 -1 SHEET 1 R 4 GLN D 5 SER D 9 0 SHEET 2 R 4 LEU D 20 SER D 27 -1 SHEET 3 R 4 THR D 80 MET D 85 -1 SHEET 4 R 4 PHE D 70 ASP D 75 -1 SHEET 1 S 2 LEU D 13 GLN D 15 0 SHEET 2 S 2 THR D 120 SER D 122 1 SHEET 1 T 5 THR D 117 VAL D 119 0 SHEET 2 T 5 ALA D 94 ARG D 100 -1 SHEET 3 T 5 MET D 36 ALA D 42 -1 SHEET 4 T 5 GLU D 48 ILE D 53 -1 SHEET 5 T 5 THR D 60 TYR D 62 -1 SHEET 1 U 4 MET D 142 GLN D 144 0 SHEET 2 U 4 VAL D 157 ALA D 163 -1 SHEET 3 U 4 ASP D 208 ILE D 213 -1 SHEET 4 U 4 PHE D 200 SER D 205 -1 SHEET 1 V 3 THR D 223 GLN D 228 0 SHEET 2 V 3 LEU D 171 GLN D 176 -1 SHEET 3 V 3 LYS D 183 ILE D 186 -1 SHEET 1 W 2 ALA D 99 TYR D 101 0 SHEET 2 W 2 MET D 110 TRP D 113 -1 SHEET 1 X 5 THR G 21 VAL G 27 0 SHEET 2 X 5 GLU G 117 LEU G 129 1 SHEET 3 X 5 GLY G 106 HIS G 114 -1 SHEET 4 X 5 ARG G 47 GLN G 53 -1 SHEET 5 X 5 CYS G 60 SER G 65 -1 SHEET 1 Y 4 LEU G 32 PRO G 37 0 SHEET 2 Y 4 THR G 92 LEU G 97 -1 SHEET 3 Y 4 THR G 82 ASP G 87 -1 SHEET 4 Y 4 ARG G 77 ASN G 79 -1 SHEET 1 Z 5 THR H 22 VAL H 27 0 SHEET 2 Z 5 GLU H 117 LEU H 129 1 SHEET 3 Z 5 GLY H 106 HIS H 114 -1 SHEET 4 Z 5 ARG H 47 GLN H 53 -1 SHEET 5 Z 5 CYS H 60 SER H 65 -1 SHEET 1 AA 3 LEU H 32 PRO H 37 0 SHEET 2 AA 3 THR H 92 LEU H 97 -1 SHEET 3 AA 3 THR H 82 ASP H 87 -1 SHEET 1 AB 5 THR I 22 VAL I 27 0 SHEET 2 AB 5 GLU I 117 LEU I 129 1 SHEET 3 AB 5 GLY I 106 HIS I 114 -1 SHEET 4 AB 5 ARG I 47 GLN I 53 -1 SHEET 5 AB 5 CYS I 60 SER I 65 -1 SHEET 1 AC 4 GLN I 33 PRO I 37 0 SHEET 2 AC 4 THR I 92 LEU I 97 -1 SHEET 3 AC 4 THR I 82 ASP I 87 -1 SHEET 4 AC 4 ARG I 77 ASN I 79 -1 SHEET 1 AD 5 THR J 22 VAL J 27 0 SHEET 2 AD 5 ALA J 118 LEU J 129 1 SHEET 3 AD 5 GLY J 106 LEU J 113 -1 SHEET 4 AD 5 LYS J 48 GLN J 53 -1 SHEET 5 AD 5 CYS J 60 SER J 65 -1 SHEET 1 AE 4 LEU J 32 PRO J 37 0 SHEET 2 AE 4 THR J 92 LEU J 97 -1 SHEET 3 AE 4 THR J 82 ASP J 87 -1 SHEET 4 AE 4 ARG J 77 ASN J 79 -1 SHEET 1 AF 5 THR K 21 VAL K 27 0 SHEET 2 AF 5 GLU K 117 LEU K 129 1 SHEET 3 AF 5 TYR K 108 HIS K 114 -1 SHEET 4 AF 5 ARG K 47 GLN K 53 -1 SHEET 5 AF 5 CYS K 60 SER K 65 -1 SHEET 1 AG 4 LEU K 32 PRO K 37 0 SHEET 2 AG 4 THR K 92 LEU K 97 -1 SHEET 3 AG 4 THR K 82 ASP K 87 -1 SHEET 4 AG 4 ARG K 77 ASN K 79 -1 SHEET 1 AH 5 THR00 22 VAL00 27 0 SHEET 2 AH 5 GLU00 117 LEU00 129 1 SHEET 3 AH 5 GLY00 106 HIS00 114 -1 SHEET 4 AH 5 ARG00 47 GLN00 53 -1 SHEET 5 AH 5 GLN00 61 SER00 65 -1 SHEET 1 AI 4 LEU00 32 PRO00 37 0 SHEET 2 AI 4 THR00 92 LEU00 97 -1 SHEET 3 AI 4 THR00 82 ASP00 87 -1 SHEET 4 AI 4 ARG00 77 ASN00 79 -1 SHEET 1 AJ 4 GLN E 5 SER E 9 0 SHEET 2 AJ 4 SER E 19 SER E 27 -1 SHEET 3 AJ 4 THR E 80 ASN E 86 -1 SHEET 4 AJ 4 PHE E 70 ASP E 75 -1 SHEET 1 AK 6 GLY E 12 VAL E 14 0 SHEET 2 AK 6 THR E 117 VAL E 121 1 SHEET 3 AK 6 ALA E 94 ARG E 100 -1 SHEET 4 AK 6 MET E 36 ALA E 42 -1 SHEET 5 AK 6 LEU E 47 ILE E 53 -1 SHEET 6 AK 6 THR E 60 TYR E 62 -1 SHEET 1 AL 4 MET E 142 GLN E 144 0 SHEET 2 AL 4 VAL E 157 ALA E 163 -1 SHEET 3 AL 4 ASP E 208 ILE E 213 -1 SHEET 4 AL 4 PHE E 200 GLY E 204 -1 SHEET 1 AM 2 SER E 148 ALA E 151 0 SHEET 2 AM 2 LYS E 241 ILE E 244 1 SHEET 1 AN 3 THR E 223 GLN E 228 0 SHEET 2 AN 3 LEU E 171 GLN E 176 -1 SHEET 3 AN 3 LYS E 183 ILE E 186 -1 SHEET 1 AO 2 ALA E 99 TYR E 101 0 SHEET 2 AO 2 MET E 110 TRP E 113 -1 SHEET 1 AP 4 GLN F 5 SER F 9 0 SHEET 2 AP 4 LEU F 20 SER F 27 -1 SHEET 3 AP 4 THR F 80 MET F 85 -1 SHEET 4 AP 4 PHE F 70 ASP F 75 -1 SHEET 1 AQ 2 LEU F 13 GLN F 15 0 SHEET 2 AQ 2 THR F 120 SER F 122 1 SHEET 1 AR 5 THR F 117 VAL F 119 0 SHEET 2 AR 5 ALA F 94 ALA F 99 -1 SHEET 3 AR 5 MET F 36 GLN F 41 -1 SHEET 4 AR 5 GLU F 48 ILE F 53 -1 SHEET 5 AR 5 THR F 60 TYR F 62 -1 SHEET 1 AS 3 MET F 142 GLN F 144 0 SHEET 2 AS 3 VAL F 157 ALA F 163 -1 SHEET 3 AS 3 ASP F 208 ILE F 213 -1 SHEET 1 AT 2 SER F 148 ALA F 151 0 SHEET 2 AT 2 LYS F 241 ILE F 244 1 SHEET 1 AU 3 THR F 223 GLN F 228 0 SHEET 2 AU 3 LEU F 171 GLN F 176 -1 SHEET 3 AU 3 LYS F 183 ILE F 186 -1 SHEET 1 AV 2 ALA F 99 TYR F 101 0 SHEET 2 AV 2 MET F 110 TRP F 113 -1 SSBOND 1 CYS A 24 CYS A 98 1555 1555 2.03 SSBOND 2 CYS A 161 CYS A 226 1555 1555 2.03 SSBOND 3 CYS B 24 CYS B 98 1555 1555 2.03 SSBOND 4 CYS B 161 CYS B 226 1555 1555 2.03 SSBOND 5 CYS C 24 CYS C 98 1555 1555 2.03 SSBOND 6 CYS C 161 CYS C 226 1555 1555 2.03 SSBOND 7 CYS D 24 CYS D 98 1555 1555 2.03 SSBOND 8 CYS D 161 CYS D 226 1555 1555 2.03 SSBOND 9 CYS G 36 CYS G 110 1555 1555 2.03 SSBOND 10 CYS G 51 CYS G 60 1555 1555 2.03 SSBOND 11 CYS H 36 CYS H 110 1555 1555 2.03 SSBOND 12 CYS H 51 CYS H 60 1555 1555 2.03 SSBOND 13 CYS I 36 CYS I 110 1555 1555 2.03 SSBOND 14 CYS I 51 CYS I 60 1555 1555 2.03 SSBOND 15 CYS J 36 CYS J 110 1555 1555 2.03 SSBOND 16 CYS J 51 CYS J 60 1555 1555 2.03 SSBOND 17 CYS K 36 CYS K 110 1555 1555 2.03 SSBOND 18 CYS K 51 CYS K 60 1555 1555 2.04 SSBOND 19 CYS00 36 CYS00 110 1555 1555 2.03 SSBOND 20 CYS00 51 CYS00 60 1555 1555 2.03 SSBOND 21 CYS E 24 CYS E 98 1555 1555 2.03 SSBOND 22 CYS E 161 CYS E 226 1555 1555 2.03 SSBOND 23 CYS F 24 CYS F 98 1555 1555 2.03 SSBOND 24 CYS F 161 CYS F 226 1555 1555 2.03 LINK ND2 ASN H 79 C1 NAG H 201 1555 1555 1.44 LINK ND2 ASN J 79 C1 NAG J 201 1555 1555 1.44 LINK ND2 ASN K 79 C1 NAG K 201 1555 1555 1.44 LINK ND2 ASN00 79 C1 NAG00 201 1555 1555 1.44 CISPEP 1 GLY G 58 PRO G 59 0 -0.92 CISPEP 2 GLY H 58 PRO H 59 0 -0.90 CISPEP 3 GLY I 58 PRO I 59 0 -1.80 CISPEP 4 GLY J 58 PRO J 59 0 -4.53 CISPEP 5 GLY K 58 PRO K 59 0 3.33 CISPEP 6 GLY00 58 PRO00 59 0 -1.23 CRYST1 167.510 180.770 125.510 90.00 90.00 90.00 P 21 21 2 24 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.005970 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005532 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007967 0.00000